ID   SYQ_CUPTR               Reviewed;         585 AA.
AC   B3R5N3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Glutamine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00126};
DE            EC=6.1.1.18 {ECO:0000255|HAMAP-Rule:MF_00126};
DE   AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00126};
DE            Short=GlnRS {ECO:0000255|HAMAP-Rule:MF_00126};
GN   Name=glnS {ECO:0000255|HAMAP-Rule:MF_00126};
GN   OrderedLocusNames=RALTA_A2274;
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1;
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC         glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC         Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC         ChEBI:CHEBI:456215; EC=6.1.1.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00126};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00126}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00126}.
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DR   EMBL; CU633749; CAQ70208.1; -; Genomic_DNA.
DR   RefSeq; WP_012353512.1; NC_010528.1.
DR   AlphaFoldDB; B3R5N3; -.
DR   SMR; B3R5N3; -.
DR   GeneID; 29762244; -.
DR   KEGG; cti:RALTA_A2274; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_001882_2_3_4; -.
DR   BioCyc; CTAI977880:RALTA_RS11030-MONOMER; -.
DR   Proteomes; UP000001692; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00807; GlnRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00126; Gln_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004514; Gln-tRNA-synth.
DR   InterPro; IPR022861; Gln_tRNA_ligase_bac.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR   InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR   InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR049437; tRNA-synt_1c_C2.
DR   NCBIfam; TIGR00440; glnS; 1.
DR   PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..585
FT                   /note="Glutamine--tRNA ligase"
FT                   /id="PRO_1000095487"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   MOTIF           299..303
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         52..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         58..64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         84
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         238
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         257
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         292..293
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
SQ   SEQUENCE   585 AA;  66312 MW;  C651D57FB0F16A44 CRC64;
     MSHDNKPTDS NPAASNFLRS IIDQDLAAGT YAGRQDKQGE PLPTVITRFP PEPNGYLHIG
     HAKSICLNFG LARDYGGRCH LRFDDTNPVK EDTEYVESII DAVHWLGFSW DSEGKDGQKQ
     PHLYYASDYF DQLYAFAETL IERGAAYVDS QSAEQIAASR GNFSEPGKPS PFRDRSVEEN
     LQLFRDMRAG KYADGEHVLR AKIDMAAPNI VMRDPVLYRI RHAHHHRTGD KWCIYPMYDF
     THCISDALEN ITHSLCTLEF ENNRPLYDWV LEHLRDSGVF RDPLPHQYEF ARLNLTYAIT
     SKRKLKQLVD EQRVDGWDDP RMPTLVGVRR RGYTPESIQL FCDRVGVAKA DSWIDMSTLE
     GSVRDDLDGR AARGVAVLDP LKLIIDNYPE GQSEECSAPV HPKKPELGKR VFPLSRELWI
     EREDFNETPP KGYFRLFPGN KVRLKYGYVI ECTGVDKDAD GNVIAVHASY LPDTKSGTPG
     ADSVKVKGVI HWVSAAHAYE AEVRLYDRLF NDPNPDAGGK NFLDALNPDS KQVITAYLEP
     GLREAQPEDR FQFERHGYFV ADRSDSTPGK PVFNRIVGLK DSWGK
//